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show all sequences of 2.3.1.37

Molecular expression and characterization of erythroid-specific 5-aminolevulinate synthase gain-of-function mutations causing X-linked protoporphyria

Bishop, D.F.; Tchaikovskii, V.; Nazarenko, I.; Desnick, R.J.; Mol. Med. 19, 18-25 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of MBP-fusion wild-type and mutant enzymes
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
F557X
site-directed mutagenesis, a ALAS2 exon 11, c.1670-1671TC>GA mutation
Homo sapiens
additional information
generation of two deletion mutants DELTAAT and DELTAAGTG enzymes. Compared to the purified wild-type enzyme, the deletion mutants show 1.8 and 3.1fold increased activity,respectively, compared to the wild-type enzyme
Homo sapiens
Q548X
naturally occuring mutation involved in X-linked protoporphyria, 1.6fold increased activity compared to the wild-type enzyme. The increased activity Q548X enzyme does not bind to succinyl-CoA synthetase
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0357
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant DELTAAGTG
Homo sapiens
0.0398
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant DELTAAT
Homo sapiens
0.0401
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant DELTAG
Homo sapiens
0.0407
-
succinyl-CoA
pH 7.4, 37C, recombinant wild-type enzyme
Homo sapiens
7.5
-
glycine
pH 7.4, 37C, recombinant mutant DELTAAGTG
Homo sapiens
7.7
-
glycine
pH 7.4, 37C, recombinant mutant F557X
Homo sapiens
9.3
-
glycine
pH 7.4, 37C, recombinant wild-type enzyme
Homo sapiens
12
-
glycine
pH 7.4, 37C, recombinant mutant Q548X
Homo sapiens
13
-
glycine
pH 7.4, 37C, recombinant mutant DELTAAT
Homo sapiens
13.5
-
glycine
pH 7.4, 37C, recombinant mutant DELTAG
Homo sapiens
36.3
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant F557X
Homo sapiens
52.4
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant Q548X
Homo sapiens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
x * 54000, recombinant wild-type enzyme, SDS-PAGE, x * 52000, recombinant mutant F557X, SDS-PAGE
Homo sapiens
54000
-
x * 54000, recombinant wild-type enzyme, SDS-PAGE, x * 52000, recombinant mutant F557X, SDS-PAGE
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
succinyl-CoA + glycine
Homo sapiens
-
5-aminolevulinate + CoA + CO2
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P22557
gene alas2
-
Purification (Commentary)
Commentary
Organism
recombinant MBP-fusion wild-type and mutant enzymes 29-114fold by amylose affinity chromatography and gel filtration
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
succinyl-CoA + glycine
-
736819
Homo sapiens
5-aminolevulinate + CoA + CO2
-
-
-
r
Subunits
Subunits
Commentary
Organism
?
x * 54000, recombinant wild-type enzyme, SDS-PAGE, x * 52000, recombinant mutant F557X, SDS-PAGE
Homo sapiens
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Homo sapiens
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
comparison of thermostability of wild-type and mutant ALAS2 aApoenzymes, overview
Homo sapiens
45
-
t1/2 of the wild-type is 11.7 min, and t1/2 of mutant enzymes are between 3.8 and 12.8 min
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
dependent on, wild-type Km is 0.0000215 nM, Km values of mutant enzymes are between 0.0000062 nM and 0.00065 nM
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of MBP-fusion wild-type and mutant enzymes
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
dependent on, wild-type Km is 0.0000215 nM, Km values of mutant enzymes are between 0.0000062 nM and 0.00065 nM
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F557X
site-directed mutagenesis, a ALAS2 exon 11, c.1670-1671TC>GA mutation
Homo sapiens
additional information
generation of two deletion mutants DELTAAT and DELTAAGTG enzymes. Compared to the purified wild-type enzyme, the deletion mutants show 1.8 and 3.1fold increased activity,respectively, compared to the wild-type enzyme
Homo sapiens
Q548X
naturally occuring mutation involved in X-linked protoporphyria, 1.6fold increased activity compared to the wild-type enzyme. The increased activity Q548X enzyme does not bind to succinyl-CoA synthetase
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0357
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant DELTAAGTG
Homo sapiens
0.0398
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant DELTAAT
Homo sapiens
0.0401
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant DELTAG
Homo sapiens
0.0407
-
succinyl-CoA
pH 7.4, 37C, recombinant wild-type enzyme
Homo sapiens
7.5
-
glycine
pH 7.4, 37C, recombinant mutant DELTAAGTG
Homo sapiens
7.7
-
glycine
pH 7.4, 37C, recombinant mutant F557X
Homo sapiens
9.3
-
glycine
pH 7.4, 37C, recombinant wild-type enzyme
Homo sapiens
12
-
glycine
pH 7.4, 37C, recombinant mutant Q548X
Homo sapiens
13
-
glycine
pH 7.4, 37C, recombinant mutant DELTAAT
Homo sapiens
13.5
-
glycine
pH 7.4, 37C, recombinant mutant DELTAG
Homo sapiens
36.3
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant F557X
Homo sapiens
52.4
-
succinyl-CoA
pH 7.4, 37C, recombinant mutant Q548X
Homo sapiens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
x * 54000, recombinant wild-type enzyme, SDS-PAGE, x * 52000, recombinant mutant F557X, SDS-PAGE
Homo sapiens
54000
-
x * 54000, recombinant wild-type enzyme, SDS-PAGE, x * 52000, recombinant mutant F557X, SDS-PAGE
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
succinyl-CoA + glycine
Homo sapiens
-
5-aminolevulinate + CoA + CO2
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant MBP-fusion wild-type and mutant enzymes 29-114fold by amylose affinity chromatography and gel filtration
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
succinyl-CoA + glycine
-
736819
Homo sapiens
5-aminolevulinate + CoA + CO2
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 54000, recombinant wild-type enzyme, SDS-PAGE, x * 52000, recombinant mutant F557X, SDS-PAGE
Homo sapiens
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Homo sapiens
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
comparison of thermostability of wild-type and mutant ALAS2 aApoenzymes, overview
Homo sapiens
45
-
t1/2 of the wild-type is 11.7 min, and t1/2 of mutant enzymes are between 3.8 and 12.8 min
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
malfunction
X-linked protoporphyria is a erythropoietic porphyria due to gain-of-function mutations in the erythroid-specific aminolevulinate synthase gene (ALAS2). Two exon 11 small deletions, c.1699_1670DELTAAT and c.1706_1709DELTAAGTG (DELTAAGTG), that prematurely truncate or elongate the ALAS2 polypeptide, are reported to increase enzymatic activity 20 to 40fold, causing the erythroid accumulation of protoporphyrins, cutaneous photosensitivity and liver disease
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
X-linked protoporphyria is a erythropoietic porphyria due to gain-of-function mutations in the erythroid-specific aminolevulinate synthase gene (ALAS2). Two exon 11 small deletions, c.1699_1670DELTAAT and c.1706_1709DELTAAGTG (DELTAAGTG), that prematurely truncate or elongate the ALAS2 polypeptide, are reported to increase enzymatic activity 20 to 40fold, causing the erythroid accumulation of protoporphyrins, cutaneous photosensitivity and liver disease
Homo sapiens
Other publictions for EC 2.3.1.37
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735604
Ogawa-Otomo
Aminolevulinate synthase 2 med ...
Xenopus laevis
Biochem. Biophys. Res. Commun.
456
476-481
2015
-
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1
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4
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6
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1
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6
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1
1
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735684
Fratz
Human erythroid 5-aminolevulin ...
Homo sapiens
Biochemistry
54
5617-5631
2015
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-
1
-
2
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1
1
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1
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3
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1
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1
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1
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1
1
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1
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5
5
-
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-
736116
Stojanovski
Murine erythroid 5-aminolevuli ...
Mus musculus
FEBS open bio
5
824-831
2015
-
-
1
-
1
-
-
5
-
-
-
1
-
4
-
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1
1
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2
1
1
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2
1
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1
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1
1
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1
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5
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1
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1
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2
1
1
-
-
2
1
-
-
-
-
2
2
-
2
2
736491
Stojanovski
Asn-150 of murine erythroid 5- ...
Mus musculus
J. Biol. Chem.
290
30750-30761
2015
-
-
1
-
6
-
-
12
-
-
-
1
-
3
-
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1
1
-
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2
-
1
-
-
6
1
-
-
1
-
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-
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1
1
-
6
-
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-
-
12
-
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1
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1
-
-
-
-
2
-
1
-
-
6
1
-
-
-
-
2
2
-
12
12
735711
Stojanovski
Catalytically active alkaline ...
Mus musculus
Biochim. Biophys. Acta
1844
2145-2154
2014
-
-
-
-
-
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
1
-
1
-
1
2
1
1
-
-
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1
-
-
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-
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1
-
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-
1
-
-
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-
1
-
1
-
1
-
1
2
1
-
-
1
1
-
-
-
736454
Stojanovski
Unstable reaction intermediate ...
Mus musculus
J. Biol. Chem.
289
22915-22925
2014
-
-
-
-
1
-
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1
-
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1
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3
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1
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4
-
1
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1
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1
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1
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1
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1
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1
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4
-
1
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1
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1
1
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737145
Fratz
Expression of murine 5-aminole ...
Mus musculus
PLoS ONE
9
e93078
2014
-
1
1
-
4
-
1
-
1
-
-
1
-
5
-
-
-
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1
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1
1
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4
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1
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1
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1
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1
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1
2
2
1
-
-
736819
Bishop
Molecular expression and chara ...
Homo sapiens
Mol. Med.
19
18-25
2013
-
-
1
-
3
-
-
12
-
-
2
1
-
2
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1
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1
1
1
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2
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1
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1
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1
1
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3
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12
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2
1
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1
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1
1
1
-
2
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1
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1
1
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719402
Shaik
Sigma-Aminolevulinate synthase ...
Drosophila melanogaster
Eur. J. Cell Biol.
91
204-215
2012
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-
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1
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-
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1
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1
1
-
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719419
Kadirvel
The carboxyl-terminal region o ...
Homo sapiens
Exp. Hematol.
40
477-486.e1
2012
-
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1
-
4
-
-
-
-
-
-
-
-
3
-
-
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1
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1
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1
1
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4
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1
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718696
Turbeville
Functional asymmetry for the a ...
Mus musculus
Arch. Biochem. Biophys.
511
107-117
2011
-
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1
-
1
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-
8
-
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1
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1
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1
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4
1
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1
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1
1
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1
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8
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1
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1
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4
1
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718890
Zhang
Hypoxic induction of human ery ...
Homo sapiens
Biochemistry
50
1194-1202
2011
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2
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2
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2
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2
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2
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720074
Kiatpapan
Production of 5-aminolevulinic ...
Acidipropionibacterium acidipropionici
J. Biosci. Bioeng.
111
425-428
2011
-
1
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1
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1
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703095
Huang
Erythroid 5-aminolevulinate sy ...
Homo sapiens
Cell Biochem. Funct.
28
122-125
2010
-
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-
-
-
-
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1
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1
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1
1
-
-
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703855
Okano
Indispensable function for emb ...
Mus musculus
Genes Cells
15
77-89
2010
-
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-
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4
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9
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9
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1
1
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704690
Lendrihas
Serine 254 enhances an induced ...
Mus musculus
J. Biol. Chem.
285
3351-3359
2010
-
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2
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6
-
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6
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1
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1
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3
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2
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1
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486859
Hunter
Lysine-313 of 5-aminolevulinat ...
Mus musculus
Biochemistry
38
3711-3718
1999
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2
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2
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4
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1
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3
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486855
Tan
The role of tyrosine 121 in co ...
Mus musculus
Protein Sci.
7
1208-1213
1998
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1
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2
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6
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1
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5
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1
1
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1
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3
1
1
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1
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1
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6
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1
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1
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3
1
1
-
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486856
Gong
Aspartate-279 in aminolevulina ...
Mus musculus
Biochemistry
37
3509-3517
1998
-
-
1
-
2
-
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4
-
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5
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1
1
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1
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2
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1
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1
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2
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486857
Tan
Role of arginine 439 in substr ...
Mus musculus
Biochemistry
37
1478-1484
1998
-
-
1
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4
-
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8
-
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4
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1
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4
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1
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1
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8
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1
-
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4
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-
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486853
Dailey
Expression and purification of ...
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus
Methods Enzymol.
281
336-340
1997
-
-
-
-
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4
4
2
-
4
2
5
-
7
-
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1
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4
-
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9
3
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1
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4
-
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4
-
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4
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4
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2
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4
2
5
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1
-
4
-
-
9
3
-
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1
-
-
-
-
-
-
-
-
-
-
486854
Zavgorodnyaya
Yeast 5-aminolevulinate syntha ...
Saccharomyces cerevisiae
Plant J.
12
169-178
1997
-
1
1
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1
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1
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5
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1
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2
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1
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1
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1
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1
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2
-
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-
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-
-
-
486851
Gong
Mutations at a glycine loop in ...
Mus musculus, Rattus norvegicus
Biochemistry
35
14109-14117
1996
-
-
1
-
4
-
-
10
-
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5
-
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1
1
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2
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2
5
-
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2
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1
2
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4
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10
-
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1
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-
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2
-
-
-
2
5
-
-
-
-
-
-
-
-
-
-
486852
Tan
Active site of 5-aminolevulina ...
Mus musculus, Saccharomyces cerevisiae
Biochemistry
35
8934-8941
1996
-
-
1
-
5
-
-
4
-
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4
2
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8
-
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1
2
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4
4
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2
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1
2
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5
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4
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4
2
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1
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-
-
4
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486849
Ferreira
Aminolevulinate synthase: lysi ...
Mus musculus
Protein Sci.
4
1001-1006
1995
-
-
1
-
3
-
-
-
-
-
-
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4
-
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1
1
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1
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1
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1
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1
1
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3
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1
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1
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-
-
-
-
1
-
-
-
-
-
-
-
-
-
486850
Ferreira
5-Aminolevulinate synthase and ...
Agrobacterium tumefaciens, Aspergillus nidulans, Bradyrhizobium japonicum, Euglena gracilis, Gallus gallus, Homo sapiens, Mus musculus, Paracoccus denitrificans, Rattus norvegicus, Rhodobacter capsulatus, Rhodobacter sphaeroides, Saccharomyces cerevisiae, Sinorhizobium meliloti
J. Bioenerg. Biomembr.
27
151-159
1995
2
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9
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2
7
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4
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11
6
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17
-
-
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8
-
10
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14
-
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13
-
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2
-
9
13
-
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2
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7
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4
-
11
6
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10
-
-
14
-
-
-
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-
-
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-
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-
486824
Ferreira
Expression of mammalian 5-amin ...
Mus musculus
J. Biol. Chem.
268
584-590
1993
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1
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2
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1
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4
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1
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1
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2
1
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1
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1
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1
1
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2
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1
1
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1
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1
-
2
1
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-
-
1
-
-
-
-
-
-
-
-
-
-
486847
Lake-Bullock
Biphasic ordered induction of ...
Mus musculus
Mol. Cell. Biol.
13
7122-7132
1993
3
-
1
-
1
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2
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2
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2
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3
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1
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1
1
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1
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2
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3
-
-
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486848
Munakata
Purification and structure of ...
Rattus norvegicus
J. Biochem.
114
103-111
1993
1
-
1
-
-
-
1
2
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3
-
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2
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1
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1
1
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1
1
1
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1
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1
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1
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1
1
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1
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2
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3
-
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1
-
1
1
-
1
1
1
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-
-
1
-
-
-
-
-
-
-
-
-
486808
Bishop
Human delta-aminolevulinate sy ...
Homo sapiens
Genomics
7
207-214
1990
-
-
-
-
-
-
-
-
1
-
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1
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2
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1
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2
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1
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1
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1
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1
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1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486814
Ades
Properties of chicken erythroc ...
Gallus gallus
Int. J. Biochem.
20
965-969
1988
-
-
-
-
-
-
1
2
1
-
2
-
-
3
-
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1
-
-
4
-
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1
1
-
-
-
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1
-
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1
-
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-
-
-
-
1
-
-
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1
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2
1
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2
-
-
-
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1
-
4
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
486815
Viale
-
Extraction and characterizatio ...
Rhodopseudomonas palustris
Comp. Biochem. Physiol. B
87
607-613
1987
1
-
-
-
-
-
2
1
-
-
1
-
-
1
-
-
-
-
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1
-
2
2
1
1
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-
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1
-
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1
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1
-
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1
-
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-
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2
-
1
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1
-
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1
-
2
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
486816
Fernandez
Trout (Salmo gairdenri R.) liv ...
Oncorhynchus mykiss
Comp. Biochem. Physiol. B
86
245-249
1987
-
-
-
-
-
-
-
-
2
-
2
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
1
-
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-
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1
-
-
-
-
-
-
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2
-
2
-
-
-
-
-
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2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
486818
Borthwick
Purification of hepatic mitoch ...
Gallus gallus, Rattus norvegicus
Methods Enzymol.
123
395-401
1986
-
-
-
-
-
-
-
-
6
-
-
2
-
2
-
-
2
-
-
4
2
4
4
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
6
-
-
2
-
-
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2
-
4
2
4
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
486819
Jordan
Purification of 5-aminolevulin ...
Rhodobacter sphaeroides
Methods Enzymol.
123
435-443
1986
-
-
-
-
-
-
5
-
-
-
2
-
-
1
-
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1
1
-
-
1
-
5
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
5
-
-
-
-
2
-
-
-
-
1
-
-
1
-
5
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
486839
Sato
-
Purification and some properti ...
Rhodobacter sphaeroides, Serratia plymuthica
Agric. Biol. Chem.
49
3415-3421
1985
2
-
-
-
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4
2
4
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2
-
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2
-
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2
-
-
-
2
1
2
-
2
-
-
-
2
-
-
2
-
-
-
2
-
-
2
-
-
4
-
2
-
4
-
-
2
-
-
-
-
2
-
-
2
1
2
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
486840
Sato
-
Occurence and some properties ...
Serratia plymuthica
Agric. Biol. Chem.
49
3423-3428
1985
-
-
-
-
-
-
-
-
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1
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1
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1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
1
-
-
-
-
-
-
-
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-
1
-
-
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1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
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-
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486835
Volland
Isolation and properties of 5- ...
Saccharomyces cerevisiae
Eur. J. Biochem.
142
551-557
1984
-
-
-
-
-
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4
2
2
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2
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2
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-
1
-
-
-
1
-
1
1
1
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
2
2
-
2
-
-
-
-
1
-
-
1
-
1
1
1
-
-
-
1
1
-
-
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-
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486823
Scotto
The characterization and submi ...
Rattus norvegicus
J. Biol. Chem.
258
81-90
1983
-
-
-
-
-
-
-
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3
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2
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-
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2
-
-
1
-
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-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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486836
Borthwick
Purification of 5-aminolaevuli ...
Gallus gallus
Eur. J. Biochem.
129
615-620
1983
-
-
-
-
-
-
-
-
1
-
1
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1
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1
-
-
2
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
1
-
-
-
-
1
-
2
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486838
Srivastava
Purification of rat liver mito ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
109
305-312
1982
-
-
-
-
-
-
-
-
1
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2
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1
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1
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1
1
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1
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
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-
-
1
-
2
-
-
-
-
1
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486817
Kreit
Control of 5-aminolevulinic ac ...
Rhodospirillum rubrum
Biochimie
63
439-444
1981
1
-
-
-
-
-
4
-
-
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1
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4
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1
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-
-
-
-
1
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-
-
-
-
1
-
-
1
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
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1
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-
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486822
Simpson
Purification of a specific act ...
Rattus norvegicus
J. Biol. Chem.
255
1630-1634
1980
2
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-
-
-
-
-
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2
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4
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2
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-
-
-
-
2
-
-
1
1
-
-
-
-
1
-
-
1
-
-
-
2
-
-
1
-
-
-
-
-
-
-
2
-
4
-
-
-
-
-
-
2
-
-
1
1
-
-
-
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1
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486834
Nakakuki
Purification and some properti ...
Rattus norvegicus
J. Biol. Chem.
255
1738-1745
1980
-
-
-
-
-
-
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3
3
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2
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2
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1
-
-
2
1
-
1
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
3
3
-
2
-
-
-
-
1
-
2
1
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
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486825
Davies
Control of 5-aminolaevulinate ...
Rhodobacter sphaeroides
Biochem. J.
177
649-659
1979
-
-
-
-
-
-
-
-
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3
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1
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1
-
-
-
1
-
1
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
1
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
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486826
Davies
Control of 5-aminolaevulinate ...
Rhodobacter sphaeroides
Biochem. J.
177
661-671
1979
-
-
-
-
-
-
-
-
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-
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1
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1
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-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486833
Paterniti
delta-Aminolevulinic acid synt ...
Rattus norvegicus
J. Biol. Chem.
254
6112-6118
1979
-
-
-
-
-
-
3
1
2
2
2
-
-
2
-
-
1
-
-
2
1
1
1
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
1
2
2
2
-
-
-
-
1
-
2
1
1
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
486837
Ohashi
Purification and some properti ...
Rattus norvegicus
J. Biochem.
85
239-247
1979
-
-
-
-
-
-
2
2
2
2
2
-
-
2
-
-
1
-
-
2
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
2
2
2
2
-
-
-
-
1
-
2
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486821
Nandi
Studies on delta-aminolevulini ...
Rhodobacter sphaeroides
J. Biol. Chem.
253
8872-8877
1978
-
-
-
-
-
-
4
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
1
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486827
Ibrahim
Hemin feedback inhibition at r ...
Oryctolagus cuniculus
Biochem. Biophys. Res. Commun.
80
722-728
1978
-
-
-
-
-
-
1
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486832
Whiting
delta-Aminolevulinic acid synt ...
Gallus gallus
J. Biol. Chem.
251
1340-1346
1976
-
-
-
-
-
-
4
-
-
4
2
-
-
1
-
-
1
-
-
2
1
2
1
1
-
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
4
1
-
-
4
2
-
-
-
-
1
-
2
1
2
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486831
Clement-Metral
5-Aminolevulinic-acid syntheta ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides Y
Eur. J. Biochem.
59
73-77
1975
-
-
-
-
-
-
2
-
-
-
1
-
-
6
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
1
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486830
Hayasaka
Control of delta-aminolevulina ...
Rhodobacter sphaeroides
J. Biochem.
76
157-168
1974
2
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486841
Murthy
Solubilization and partial pur ...
Rattus norvegicus
Biochim. Biophys. Acta
350
240-246
1974
1
-
-
-
-
-
3
-
2
-
-
-
-
2
-
-
1
-
-
4
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
3
-
-
2
-
-
-
-
-
-
1
-
4
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486809
Ramaswamy
delta-Aminolevulinic acid synt ...
Solanum tuberosum
Biochim. Biophys. Acta
293
269-277
1973
2
-
-
-
-
-
4
-
-
1
-
1
-
1
-
-
-
-
-
1
2
1
2
-
1
-
1
-
1
-
-
1
-
-
-
2
-
-
1
-
-
-
-
4
-
-
-
1
-
1
-
-
-
-
-
1
2
1
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
486810
Tait
Aminolaevulinate synthetase of ...
Paracoccus denitrificans
Biochem. J.
131
389-403
1973
-
-
-
-
-
-
4
3
-
-
1
-
-
1
-
-
1
-
-
1
2
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
3
-
-
1
-
-
-
-
1
-
1
2
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
486844
Fanica-Gaignier
5-Aminolevulinic-acid syntheta ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides Y
Eur. J. Biochem.
40
13-18
1973
-
-
-
-
-
-
-
-
-
-
2
-
-
6
-
-
1
-
-
-
2
1
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
2
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
486845
Fanica-Gaignier
5-Aminolevulinic-acid syntheta ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides Y
Eur. J. Biochem.
40
19-24
1973
-
-
-
-
-
-
4
1
-
-
-
-
-
6
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
1
3
-
-
-
-
-
1
-
-
-
-
4
3
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486812
Scholnick
Souble delta-aminolevulinic ac ...
Rattus norvegicus
J. Biol. Chem.
247
4126-4131
1972
1
-
-
-
-
1
-
4
1
1
2
1
-
1
-
-
1
-
-
1
1
-
3
-
-
-
-
-
2
-
1
1
-
-
-
1
-
-
1
-
-
1
-
-
-
4
1
1
2
1
-
-
-
1
-
1
1
-
3
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
486813
Scholnick
Soluble delta-aminolevulinic a ...
Rattus norvegicus
J. Biol. Chem.
247
4132-4137
1972
-
-
-
-
-
-
14
-
1
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
14
1
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486820
Jordan
-
delta-Aminolevulinic acid synt ...
Cavia porcellus, Gallus gallus, Homo sapiens, no activity in Chromatium sp., Novispirillum itersonii, Oryctolagus cuniculus, Propionibacterium freudenreichii subsp. shermanii, Rattus norvegicus, Rhodobacter sphaeroides, Rhodospirillum rubrum, Saccharomyces cerevisiae, Spinacia oleracea
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
339-356
1972
3
-
-
-
-
-
110
9
13
-
5
21
-
12
-
-
3
10
-
10
8
-
62
-
-
-
2
-
-
-
-
11
-
-
-
3
-
-
11
-
-
-
-
110
-
9
13
-
5
21
-
-
-
3
-
10
8
-
62
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
486828
Porra
The nature of the inhibition o ...
Rhodobacter sphaeroides
Arch. Biochem. Biophys.
148
37-43
1972
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486842
Yubisui
delta-Aminolevulinic acid synt ...
Rhodobacter sphaeroides
Arch. Biochem. Biophys.
150
77-85
1972
1
-
-
-
-
1
12
-
-
-
1
-
-
1
-
-
1
-
-
-
1
1
1
-
-
-
-
-
1
-
-
1
-
-
-
1
-
-
1
-
-
1
-
12
-
-
-
-
1
-
-
-
-
1
-
-
1
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
486843
Whiting
Purification and properties of ...
Cavia porcellus, Rattus norvegicus
J. Biol. Chem.
247
6818-6826
1972
-
-
-
-
-
-
2
3
5
-
2
-
-
2
-
-
2
-
-
2
-
2
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
3
5
-
2
-
-
-
-
2
-
2
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486811
Warnick
Regulation of prophyrin biosyn ...
Rhodobacter sphaeroides
J. Biol. Chem.
246
6880-6885
1971
1
-
-
-
-
1
3
-
-
1
1
-
-
1
-
-
1
-
-
-
1
2
2
2
-
-
1
-
1
-
-
1
-
-
-
1
-
-
1
-
-
1
-
3
-
-
-
1
1
-
-
-
-
1
-
-
1
2
2
2
-
-
1
-
1
-
-
-
-
-
-
-
-
-
486829
Tuboi
Control of delta-aminolevulina ...
Rhodobacter sphaeroides
Arch. Biochem. Biophys.
146
282-290
1971
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-